Numerous metabolic pathways generate free ADP-ribose at many locations
within cells. The metabolic fates of this nucleotide are poorly under
stood and measurement of it in situ is technically difficult at presen
t. Yet considerable evidence has accumulated implicating that protein
glycation by ADP-ribose can occur. This evidence is reviewed here alon
g with recent developments in characterizing the chemistry of this rea
ction and the application of this information to the identification of
this posttranslational modification in protein in situ.